ID A0A091I1J2_CALAN Unreviewed; 362 AA.
AC A0A091I1J2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 29.
DE RecName: Full=protein phosphatase methylesterase-1 {ECO:0000256|ARBA:ARBA00013111};
DE EC=3.1.1.89 {ECO:0000256|ARBA:ARBA00013111};
DE Flags: Fragment;
GN ORFNames=N300_09780 {ECO:0000313|EMBL:KFP01300.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP01300.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFP01300.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP01300.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Demethylates proteins that have been reversibly
CC carboxymethylated. Demethylates PPP2CB (in vitro) and PPP2CA. Binding
CC to PPP2CA displaces the manganese ion and inactivates the enzyme.
CC {ECO:0000256|ARBA:ARBA00024698}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphatase 2A protein]-C-terminal L-leucine methyl ester +
CC H2O = [phosphatase 2A protein]-C-terminal L-leucine + H(+) +
CC methanol; Xref=Rhea:RHEA:48548, Rhea:RHEA-COMP:12134, Rhea:RHEA-
CC COMP:12135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:90516, ChEBI:CHEBI:90517; EC=3.1.1.89;
CC Evidence={ECO:0000256|ARBA:ARBA00000906};
CC -!- SUBUNIT: Binds PPP2CA and PPP2CB. {ECO:0000256|ARBA:ARBA00011604}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC {ECO:0000256|ARBA:ARBA00008645}.
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DR EMBL; KL218027; KFP01300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091I1J2; -.
DR STRING; 9244.A0A091I1J2; -.
DR Proteomes; UP000054308; Unassembled WGS sequence.
DR GO; GO:0051723; F:protein methylesterase activity; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR016812; PPase_methylesterase_euk.
DR PANTHER; PTHR14189:SF0; PROTEIN PHOSPHATASE METHYLESTERASE 1; 1.
DR PANTHER; PTHR14189; PROTEIN PHOSPHATASE METHYLESTERASE-1 RELATED; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PIRSF; PIRSF022950; PPase_methylesterase_euk; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054308}.
FT DOMAIN 61..344
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF12697"
FT REGION 234..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 135
FT /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT ACT_SITE 160
FT /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT ACT_SITE 331
FT /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP01300.1"
FT NON_TER 362
FT /evidence="ECO:0000313|EMBL:KFP01300.1"
SQ SEQUENCE 362 AA; 39982 MW; F185F9D107D24AB9 CRC64;
PGRKRDFSPV LWSQYFESME DVVVENETGK DISFFFSLIE LIFSDRDTFR IYKSGLEGPV
LLLLHGGGHS ALSWAVFTVT RQEAMVSSCA RGGLGETKVR NPEDLSAETM SKDVGNVVEA
LYGDLPPPIM LIGHSMGGAI AVHTAVANLV PSLLGLCMID VVEGTAMDAL NSMQNFLRSR
PKTFKSLENA IEWSVKSGQI RNLESARVSM VGQVKQCEGA ASPECPKAIV EGIIEEEEED
EEGEEGGGSV NKRKKEDDTE TKKEHLYTWR IELAKTEKYW DGWFRGLSNL FLSCPTPKLL
LLAGVDRLDK DLTIGQMQGK FQMQVLPQCG HAVHEDAPDK VAEAVATFLI RHRFTEPIGG
FQ
//
